D-Sedoheptulose-7-phosphate: D-Glyceraldehyde-3-phosphate Glycolaldehydetransferase and D-Ribulose-5-phosphate 3-Epimerase Mutants of a Bacillus Species
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منابع مشابه
Preparative scale enzymatic synthesis of D-sedoheptulose-7-phosphate from -hydroxypyruvate and D-ribose-5-phosphate
An enzymatic method for ready access to D-sedoheptulose-7-phosphate on a preparative scale was developed, based on the irreversible transketolase-catalyzed reaction: β-hydroxypyruvate + D-ribose-5phosphate → D-sedoheptulose-7-phosphate. D-Sedoheptulose-7-phosphate disodium salt was obtained in 81% overall yield determined using a standard curve obtained by LC/MS/MS.
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The crystal structure of D-ribulose 5-phosphate 3-epimerase (RPE) from the cyanobacterium Synechocystis was determined by X-ray crystallography to 1.6 A resolution. The enzyme, which catalyzes the epimerization of D-ribulose 5-phosphate and D-xylulose 5-phosphate, assembles as a hexamer of (beta/alpha)(8)-barrels in the crystallographic asymmetric unit. The active site is highly similar to thos...
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d-Arabinose-5-phosphate and d-sedoheptulose-7-phosphate were found to be substrates, although not inducers, of the hexose phosphate transport system of Salmonella typhimurium. Transport of these two sugar phosphates by wild-type strains required preinduction of the hexose phosphate transport system. A mutant of S. typhimurium constitutive for this system also transported d-arabinose-5-phosphate...
متن کاملThe active chemical state of D-glyceraldehyde 3-phosphate in its reactions with D-glyceraldehyde 3-phosphate dehydrogenase, aldolase and triose phosphate isomerase.
Glyceraldehyde 3-phosphate exists as the geminal diol and the free aldehyde in the molar ratio 29:1 in aqueous solution. The rate constant of the conversion of diol into aldehyde is 8.7x10(-2)sec.(-1) in the pH range 7.3-8.6 at 20 degrees . The free aldehyde is the substrate for d-glyceraldehyde 3-phosphate dehydrogenase. Over a wide concentration range of enzyme the rate of conversion of diol ...
متن کاملD-glyceraldehyde 3-phosphate dehydrogenases of higher plants.
The d-glyceraldehyde 3-P dehydrogenases of spinach leaf, pea seed, and pea shoot were purified. The NADP and NAD-linked enzymes of either spinach leaves and pea shoots could not be separated. Changes in the ratio of NADP- to NAD-linked activity of the spinach leaf and pea shoot enzymes were observed during both purification and storage of crude extracts. The spinach leaf, pea shoot, and pea see...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1974
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.38.1305